ID X8DH48_9MYCO Unreviewed; 292 AA.
AC X8DH48;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Diacylglycerol kinase {ECO:0000313|EMBL:EUA67371.1};
DE EC=2.7.1.107 {ECO:0000313|EMBL:EUA67371.1};
GN Name=dagK {ECO:0000313|EMBL:EUA67371.1};
GN ORFNames=I540_4583 {ECO:0000313|EMBL:EUA67371.1};
OS Mycobacteroides abscessus subsp. bolletii 1513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=1299321 {ECO:0000313|EMBL:EUA67371.1, ECO:0000313|Proteomes:UP000023351};
RN [1] {ECO:0000313|EMBL:EUA67371.1, ECO:0000313|Proteomes:UP000023351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1513 {ECO:0000313|EMBL:EUA67371.1,
RC ECO:0000313|Proteomes:UP000023351};
RA Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EUA67371.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JAOJ01000003; EUA67371.1; -; Genomic_DNA.
DR AlphaFoldDB; X8DH48; -.
DR PATRIC; fig|1299321.3.peg.4420; -.
DR Proteomes; UP000023351; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.60.200.40; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR005218; Diacylglycerol/lipid_kinase.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR045540; YegS/DAGK_C.
DR NCBIfam; TIGR00147; YegS/Rv2252/BmrU family lipid kinase; 1.
DR PANTHER; PTHR12358:SF106; LIPID KINASE YEGS; 1.
DR PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF19279; YegS_C; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EUA67371.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EUA67371.1}.
FT DOMAIN 1..129
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
SQ SEQUENCE 292 AA; 30490 MW; 1EE4BEE1EC574C4A CRC64;
MTHLTVLTNP TAGHAAAQAA EAAIAHLRAR GLTVTHHAAT SAAESHELAQ EAARTGARGI
VAAGGDGLVS IALQAVAATP VALGVIPIGT GNDCARMLDI PLSDPVAAAE VIAAGRTRVI
DAGRIQYHGD TTWFATVVAS GFDSLVNDRA NRMRWPRGRR RYDIAMALEA AKLRPLPFRI
ELDDQVIDTD VTLVAVGNGT SYGGGMRICP GAILDDGLLD VTVVAAGGRL RLLRLSPTVY
KGTHVDLPEV STFRSRRVRL YAADITAYAD GDPVAPLPVD IDVVPAALSV FA
//
